Hot debate in hot springs: Report on the second international meeting on <scp>SMC</scp> proteins

Hirano, Takeshi; Nishiyama, Tomoko; Shirahige, Katsuhiko

doi:10.1111/gtc.12539

Cited by 3 publications

(3 citation statements)

References 29 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In addition, ATP binding and hydrolysis provide the SMC complexes with motor activity that allows them to slide along the entrapped DNA molecule(s). This SMC translocation activity may progressively enlarge loops of DNA in a process termed loop extrusion (Figure 2b) [2,6,56,57,58,59,60,61,62,63]. For example, the condensin and SMC/ScpAB complexes translocate along the DNA strands leaving loop(s) behind [59,64,65].…”

Section: Introductionmentioning

confidence: 99%

SMC5/6: Multifunctional Player in Replication

Paleček

2018

Genes

View full text Add to dashboard Cite

The genome replication process is challenged at many levels. Replication must proceed through different problematic sites and obstacles, some of which can pause or even reverse the replication fork (RF). In addition, replication of DNA within chromosomes must deal with their topological constraints and spatial organization. One of the most important factors organizing DNA into higher-order structures are Structural Maintenance of Chromosome (SMC) complexes. In prokaryotes, SMC complexes ensure proper chromosomal partitioning during replication. In eukaryotes, cohesin and SMC5/6 complexes assist in replication. Interestingly, the SMC5/6 complexes seem to be involved in replication in many ways. They stabilize stalled RFs, restrain RF regression, participate in the restart of collapsed RFs, and buffer topological constraints during RF progression. In this (mini) review, I present an overview of these replication-related functions of SMC5/6.

show abstract

Section: Introductionmentioning

confidence: 99%

SMC5/6: Multifunctional Player in Replication

Paleček

2018

Genes

View full text Add to dashboard Cite

show abstract

“…Besides such a single-ring model (12)(13)(14)(15)(16)(17)(18), higher-order oligomeric cohesin conformations have also been proposed based upon the unusual genetic properties and physical self-interactions of cohesin subunits in yeast (19) and human cells (20), respectively. Therefore, it remains highly debatable whether cohesin functions as single-rings, double-rings or clusters (6,(21)(22)(23).…”

Section: Introductionmentioning

confidence: 99%

The acetyltransferase Eco1 elicits cohesin dimerization during S phase

Shi

Zhao

Zuo

et al. 2020

Journal of Biological Chemistry

View full text Add to dashboard Cite

Cohesin is a DNA-associated protein complex that forms a tripartite ring controlling sister chromatid cohesion, chromosome segregation and organization, DNA replication, and gene expression. Sister chromatid cohesion is established by the protein acetyltransferase Eco1, which acetylates two conserved lysine residues on the cohesin subunit Smc3 and thereby ensures correct chromatid separation in yeast (Saccharomyces cerevisiae) and other eukaryotes. However, the consequence of Eco1-catalyzed cohesin acetylation is unknown, and the exact nature of the cohesive state of chromatids remains controversial. Here, we show that self-interactions of the cohesin subunits Scc1/Rad21 and Scc3 occur in a DNA replication–coupled manner in both yeast and human cells. Using cross-linking MS-based and in vivo disulfide cross-linking analyses of purified cohesin, we show that a subpopulation of cohesin may exist as dimers. Importantly, upon temperature-sensitive and auxin-induced degron-mediated Eco1 depletion, the cohesin-cohesin interactions became significantly compromised, whereas deleting either the deacetylase Hos1 or the Eco1 antagonist Wpl1/Rad61 increased cohesin dimer levels by ∼20%. These results indicate that cohesin dimerizes in the S phase and monomerizes in mitosis, processes that are controlled by Eco1, Wpl1, and Hos1 in the sister chromatid cohesion-dissolution cycle. These findings suggest that cohesin dimerization is controlled by the cohesion cycle and support the notion that a double-ring cohesin model operates in sister chromatid cohesion.

show abstract

“…Besides such a single-ring model (12-18), higher-order oligomeric cohesin conformations have also been proposed based upon the unusual genetic properties and physical self-interactions of cohesin subunits in yeast (19) and human cells (20), respectively. Therefore, it remains highly debatable whether cohesin functions as single-rings, double-rings or clusters (6, 21-23).…”

Section: Introductionmentioning

confidence: 99%

The acetyltransferase Eco1 elicits cohesin dimerization during S phase

Shi

Zhao

Zuo

et al. 2020

Preprint

View full text Add to dashboard Cite

AbstractSister chromatid cohesion is established by Eco1 in S phase. Nevertheless, the exact consequence of Eco1-catalyzed acetylation is unknown, and the cohesive state remains highly controversial. Here we show that self-interactions of cohesin subunits Scc1/Rad21 and Scc3 occur in a DNA replication-coupled manner in both yeast and human. Through cross-linking mass spectrometry and VivosX analysis of purified cohesin, we show that a subpopulation of cohesin may exist as dimers. Importantly, cohesin-cohesin interaction becomes significantly compromised when Eco1 is depleted. On the other hand, deleting either deacetylase Hos1 or Eco1 antagonist Wpl1/Rad61 results in an increase (e.g., from ∼20% to 40%) of cohesin dimers. These findings suggest that cohesin dimerization is controlled by common mechanisms as the cohesion cycle, thus providing an additional layer of regulation for cohesin to execute various functions such as sister chromatid cohesion, DNA repair, gene expression, chromatin looping and high-order organization.Author SummaryCohesin is a ring that tethers sister chromatids since their synthesis during S phase till their separation in anaphase. According to the single-ring model, one ring holds twin sisters. Here we show a conserved cohesin-cohesin interaction from yeast to human. A subpopulation of cohesin is dimerized concomitantly with DNA replication. Cohesin dimerization is dependent on the acetyltransferase Eco1 and counteracted by the anti-establishment factor Wpl1 and deacetylase Hos1. Approximately 20% of cellular cohesin complexes are measured to be dimers, close to the level of Smc3 acetylation by Eco1 in vivo. These findings provide evidence to support the double-ring model in sister chromatid cohesion.

show abstract

Hot debate in hot springs: Report on the second international meeting on SMC proteins

Cited by 3 publications

References 29 publications

SMC5/6: Multifunctional Player in Replication

SMC5/6: Multifunctional Player in Replication

The acetyltransferase Eco1 elicits cohesin dimerization during S phase

The acetyltransferase Eco1 elicits cohesin dimerization during S phase

Contact Info

Product

Resources

About